Reactome | Murphy, G

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Murphy, G Show undefined attributes

created	[InstanceEdit:1013929] Jupe, S, 2010-11-12
dbId	1013917
displayName	Murphy, G
initial	G
publications	[LiteratureReference:1564207] Partial purification of collagenase and gelatinase from human polymorphonuclear leucocytes. Analysis of their actions on soluble and insoluble collagens [LiteratureReference:1564133] Metalloproteinases from rabbit bone culture medium degrade types IV and V collagens, laminin and fibronectin [LiteratureReference:1564193] Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP) [LiteratureReference:1592430] The latent collagenase and gelatinase of human polymorphonuclear neutrophil leucocytes [LiteratureReference:2157499] The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity [LiteratureReference:1592358] The 28-kDa N-terminal domain of mouse stromelysin-3 has the general properties of a weak metalloproteinase [LiteratureReference:1458419] Stromelysin, a connective tissue-degrading metalloendopeptidase secreted by stimulated rabbit synovial fibroblasts in parallel with collagenase. Biosynthesis, isolation, characterization, and substrates [LiteratureReference:1566956] Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members [LiteratureReference:1474211] Human and rat malignant-tumor-associated mRNAs encode stromelysin-like metalloproteinases [LiteratureReference:1454748] Structure and function of matrix metalloproteinases and TIMPs [LiteratureReference:1454854] Metalloproteinase inhibitors: biological actions and therapeutic opportunities [LiteratureReference:1474205] Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain [LiteratureReference:1592301] Sites of nidogen cleavage by proteases involved in tissue homeostasis and remodelling [LiteratureReference:1592360] Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases [LiteratureReference:1592463] Activation of progelatinase B (proMMP-9) by active collagenase-3 (MMP-13) [LiteratureReference:1564108] Degradation of entactin by matrix metalloproteinases. Susceptibility to matrilysin and identification of cleavage sites [LiteratureReference:1458404] Biochemical characterization of human collagenase-3 [LiteratureReference:1604688] Analysis of the role of the COOH-terminal domain in the activation, proteolytic activity, and tissue inhibitor of metalloproteinase interactions of gelatinase B [LiteratureReference:1592345] Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloproteinases [LiteratureReference:1564199] The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction [LiteratureReference:1013942] Primary megakaryocytes reveal a role for transcription factor NF-E2 in integrin alpha IIb beta 3 signaling [LiteratureReference:1602462] Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme [LiteratureReference:1602452] Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes [LiteratureReference:1592280] Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases [LiteratureReference:1592332] The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study
schemaClass	Person
surname	Murphy

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